CERT1 Knockout Cell Line (Hela)

The choice depends on whether you are studying CERT1 (ceramide transfer protein 1, COL4A3BP, STARD11)'s role as a non-vesicular ceramide transporter or modeling its functions in sphingolipid biology and emerging neurodevelopmental disease. The Knockout line is the standard tool for asking whether CERT1 is required for these processes — CERT1 is a START-domain containing protein that mediates non-vesicular transfer of ceramide from the ER to the trans-Golgi network for sphingomyelin and glucosylceramide synthesis; CERT1 has N-terminal PH domain (Golgi PI4P binding), middle FFAT motif (ER VAP binding), and C-terminal START domain (ceramide binding). Overexpression is useful for studying CERT1 in heterologous expression contexts. For sphingolipid biology research, the EDITGENE CERT1 Knockout in HeLa is highly informative — CERT1 de novo heterozygous mutations cause autosomal dominant intellectual disability syndrome (NEDMIAH, neurodevelopmental disorder with intellectual disability and seizures). Rescue with wild-type, ceramide-binding-deficient (G67E START domain), or NEDMIAH-associated CERT1 mutations enables comprehensive structure-function and disease modeling. The knockout is valuable for studying ER-Golgi non-vesicular lipid transfer and CERT1-related neurodevelopmental disorder mechanisms.

Primary applications: • Non-vesicular ceramide transfer: ER-to-Golgi ceramide transport analysis in CERT1-null cells. • Sphingolipid metabolism: sphingomyelin and glucosylceramide synthesis analysis given CERT1-dependent ceramide supply to TGN. • NEDMIAH modeling: rescue with de novo heterozygous CERT1 mutations causing intellectual disability syndrome. • ER-Golgi contact sites: ER-TGN membrane contact site analysis given CERT1's FFAT motif-PH domain bridge function. EDITGENE recommends this model for researchers investigating non-vesicular lipid transfer, sphingolipid biology, and CERT1-related neurodevelopmental disorder.

Yes. CERT1 rescue experiments are well-established for non-vesicular lipid transfer research: • Construct design: use a codon-modified CERT1 sequence with a small C-terminal tag (FLAG, HA). CERT1 has N-terminal PH domain (Golgi PI4P binding), middle FFAT motif (ER VAP-A/B binding), and C-terminal START domain (ceramide binding) — preserve all elements. • Ceramide-binding-deficient rescue: G67E mutation in the START domain abolishes ceramide binding. • PH-deficient rescue: PH domain mutations disrupt Golgi PI4P binding. • FFAT-mutant rescue: FFAT motif mutations disrupt ER VAP binding. • NEDMIAH mutation rescue: de novo heterozygous CERT1 mutations enable disease modeling. • Functional readout: rescue should restore ER-Golgi ceramide transfer and sphingomyelin synthesis. HeLa transduces efficiently with lentivirus and supports stable rescue line generation.